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Updated: Jun 8, 2026

Biophysical Characterization of Flagellar Motor Functions
Published on: January 18, 2017
Cryo-EM Structure of the Flagellar Motor Complex from Paenibacillus sp. TCA20
Sakura Onoe1, Tatsuro Nishikino1,2,3, Miki Kinoshita4,5
1Institute for Protein Research, Osaka University, Suita 565-0871, Osaka, Japan.
Abstract:
The bacterial flagellum, a complex nanomachine composed of numerous proteins, is utilized by bacteria for swimming in various environments and plays a crucial role in their survival and infection. The flagellar motor is composed of a rotor and stator complexes, with each stator unit functioning as an ion channel that converts flow from outside of cell membrane into rotational motion. Paenibacillus sp. TCA20 was discovered in a hot spring, and a structural analysis was conducted on the stator complex using cryo-electron microscopy to elucidate its function. Two of the three structures (Classes 1 and 3) were found to have structural properties typical for other stator complexes. In contrast, in Class 2 structures, the pentamer ring of the A subunits forms a C-shape, with lauryl maltose neopentyl glycol (LMNG) bound to the periplasmic side of the interface between the A and B subunits. This interface is conserved in all stator complexes, suggesting that hydrophobic ligands and lipids can bind to this interface, a feature that could potentially be utilized in the development of novel antibiotics aimed at regulating cell motility and infection.
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